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| | <StructureSection load='5zmf' size='340' side='right'caption='[[5zmf]], [[Resolution|resolution]] 3.56Å' scene=''> | | <StructureSection load='5zmf' size='340' side='right'caption='[[5zmf]], [[Resolution|resolution]] 3.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZMF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZMF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.556Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARSA1, AS1, CHLREDRAFT_132949 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zmf OCA], [http://pdbe.org/5zmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zmf RCSB], [http://www.ebi.ac.uk/pdbsum/5zmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zmf ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zmf OCA], [https://pdbe.org/5zmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zmf RCSB], [https://www.ebi.ac.uk/pdbsum/5zmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zmf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ASNA1_CHLRE ASNA1_CHLRE]] ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis (PubMed:28382961).<ref>PMID:23167510</ref> <ref>PMID:28382961</ref> | + | [https://www.uniprot.org/uniprot/ASNA1_CHLRE ASNA1_CHLRE] ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis (PubMed:28382961).<ref>PMID:23167510</ref> <ref>PMID:28382961</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, H Y]] | + | [[Category: Chang HY]] |
| - | [[Category: Hsiao, C D]] | + | [[Category: Hsiao CD]] |
| - | [[Category: Lin, T W]] | + | [[Category: Lin TW]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Chloroplast]]
| + | |
| - | [[Category: Hydrolase-transport protein complex]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
ASNA1_CHLRE ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the chloroplast. Required for the accumulation of TOC34, an essential component of the outer chloroplast membrane translocon (TOC) complex (PubMed:23167510, PubMed:28382961). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to chloroplast, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis (PubMed:28382961).[1] [2]
Publication Abstract from PubMed
Tail-anchored (TA) membrane proteins destined for the posttranslational pathway are safely delivered to the endoplasmic reticulum (ER) membrane by a well-known targeting factor, TRC40/Get3, in mammals and yeast. In contrast, the underlying mechanism for translocation of TA proteins in plants remains obscure. How this unique eukaryotic membrane-trafficking system correctly distinguishes different subsets of TA proteins destined for various organelles, including mitochondria, chloroplasts and the ER, is a key long-standing question. Here, we present crystal structures of algae ArsA1 (the Get3 homolog) in a distinct open state of nucleotide-free and AMPPNP-bound. This ~80-kDa protein possesses a monomeric architecture, with two ATPase domains in a single polypeptide chain. It is capable of binding chloroplast (TOC34 and TOC159) and mitochondrial (TOM7) TA proteins based on features of its transmembrane domain as well as the regions right before and after the transmembrane domain. Several helices located above the TA-binding groove comprise the interlocking hook-like motif implicated in TA substrate recognition by mutational analyses. Our data provide insights into the molecular basis of the highly specific selectivity of algae ArsA1 interactions with the correct sets of TA substrates before membrane targeting in plant cells. This article is protected by copyright. All rights reserved.
Structural analysis of chloroplast tail-anchored membrane protein recognition by ArsA1.,Lin TW, Chen CC, Wu SM, Chang YC, Li YC, Su YW, Hsiao CD, Chang HY Plant J. 2019 Mar 20. doi: 10.1111/tpj.14316. PMID:30891827[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Formighieri C, Cazzaniga S, Kuras R, Bassi R. Biogenesis of photosynthetic complexes in the chloroplast of Chlamydomonas reinhardtii requires ARSA1, a homolog of prokaryotic arsenite transporter and eukaryotic TRC40 for guided entry of tail-anchored proteins. Plant J. 2013 Mar;73(5):850-61. doi: 10.1111/tpj.12077. Epub 2012 Dec 28. PMID:23167510 doi:http://dx.doi.org/10.1111/tpj.12077
- ↑ Maestre-Reyna M, Wu SM, Chang YC, Chen CC, Maestre-Reyna A, Wang AH, Chang HY. In search of tail-anchored protein machinery in plants: reevaluating the role of arsenite transporters. Sci Rep. 2017 Apr 6;7:46022. doi: 10.1038/srep46022. PMID:28382961 doi:http://dx.doi.org/10.1038/srep46022
- ↑ Lin TW, Chen CC, Wu SM, Chang YC, Li YC, Su YW, Hsiao CD, Chang HY. Structural analysis of chloroplast tail-anchored membrane protein recognition by ArsA1. Plant J. 2019 Mar 20. doi: 10.1111/tpj.14316. PMID:30891827 doi:http://dx.doi.org/10.1111/tpj.14316
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